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Protein

Endoglucanase-5

Gene

egl5

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei27NucleophilePROSITE-ProRule annotation1
Active sitei134Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16505.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH45. Glycoside Hydrolase Family 45.
mycoCLAPiEGL45E_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase-5 (EC:3.2.1.4)
Alternative name(s):
Cellulase V
Endo-1,4-beta-glucanase V
Short name:
EG V
Endoglucanase V
Gene namesi
Name:egl5
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000802218 – 242Endoglucanase-5Add BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi182N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi213 ↔ 230PROSITE-ProRule annotation
Disulfide bondi224 ↔ 240PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI49976.

Structurei

3D structure databases

ProteinModelPortaliP43317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini205 – 241CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 182CatalyticAdd BLAST165

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi183 – 205Pro/Ser-rich (linker)Add BLAST23

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JAN1. Eukaryota.
ENOG410YDK7. LUCA.
OMAiCPGQATS.

Family and domain databases

Gene3Di2.40.40.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR007112. Expansin/allergen_DPBB_dom.
IPR000334. Glyco_hydro_45.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03330. DPBB_1. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS50842. EXPANSIN_EG45. 1 hit.
PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43317-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATLVLGSL IVGAVSAYKA TTTRYYDGQE GACGCGSSSG AFPWQLGIGN
60 70 80 90 100
GVYTAAGSQA LFDTAGASWC GAGCGKCYQL TSTGQAPCSS CGTGGAAGQS
110 120 130 140 150
IIVMVTNLCP NNGNAQWCPV VGGTNQYGYS YHFDIMAQNE IFGDNVVVDF
160 170 180 190 200
EPIACPGQAA SDWGTCLCVG QQETDPTPVL GNDTGSTPPG SSPPATSSSP
210 220 230 240
PSGGGQQTLY GQCGGAGWTG PTTCQAPGTC KVQNQWYSQC LP
Length:242
Mass (Da):24,411
Last modified:November 1, 1995 - v1
Checksum:iCC033FC51326C71D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33381 Genomic DNA. Translation: CAA83846.1.
PIRiS60143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33381 Genomic DNA. Translation: CAA83846.1.
PIRiS60143.

3D structure databases

ProteinModelPortaliP43317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI49976.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH45. Glycoside Hydrolase Family 45.
mycoCLAPiEGL45E_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410JAN1. Eukaryota.
ENOG410YDK7. LUCA.
OMAiCPGQATS.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16505.

Family and domain databases

Gene3Di2.40.40.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR007112. Expansin/allergen_DPBB_dom.
IPR000334. Glyco_hydro_45.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03330. DPBB_1. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS50842. EXPANSIN_EG45. 1 hit.
PS01140. GLYCOSYL_HYDROL_F45. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN5_HYPJE
AccessioniPrimary (citable) accession number: P43317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 5, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.